A0AA41WB89 · A0AA41WB89_9BACT

  • Protein
    Riboflavin biosynthesis protein RibBA
  • Gene
    ribBA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Note: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4.

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site28-29D-ribulose 5-phosphate (UniProtKB | ChEBI)
Binding site29Mg2+ 1 (UniProtKB | ChEBI)
Binding site29Mg2+ 2 (UniProtKB | ChEBI)
Binding site33D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site129Essential for DHBP synthase activity
Binding site167D-ribulose 5-phosphate (UniProtKB | ChEBI)
Site167Essential for DHBP synthase activity
Binding site255-259GTP (UniProtKB | ChEBI)
Binding site260Zn2+ (UniProtKB | ChEBI); catalytic
Binding site271Zn2+ (UniProtKB | ChEBI); catalytic
Binding site273Zn2+ (UniProtKB | ChEBI); catalytic
Binding site276GTP (UniProtKB | ChEBI)
Binding site298-300GTP (UniProtKB | ChEBI)
Binding site320GTP (UniProtKB | ChEBI)
Active site332Proton acceptor; for GTP cyclohydrolase activity
Active site334Nucleophile; for GTP cyclohydrolase activity
Binding site355GTP (UniProtKB | ChEBI)
Binding site360GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Function3,4-dihydroxy-2-butanone-4-phosphate synthase activity
Molecular FunctionGTP binding
Molecular FunctionGTP cyclohydrolase II activity
Molecular Functionmagnesium ion binding
Molecular Functionmanganese ion binding
Molecular Functionzinc ion binding
Biological Processriboflavin biosynthetic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Riboflavin biosynthesis protein RibBA

Including 2 domains:

  • Recommended name
    3,4-dihydroxy-2-butanone 4-phosphate synthase
  • EC number
  • Short names
    DHBP synthase
  • Recommended name
    GTP cyclohydrolase-2
  • EC number
  • Alternative names
    • GTP cyclohydrolase II

Gene names

    • Name
      ribBA
    • ORF names
      NET02_04680

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CFH 74404
  • Taxonomic lineage
    Bacteria > Thermomicrobiota > Thermomicrobia > Thermomicrobiales > Thermomicrobiaceae > Thermalbibacter

Accessions

  • Primary accession
    A0AA41WB89

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-204DHBP synthase
Region205-420GTP cyclohydrolase II
Domain211-376GTP cyclohydrolase II

Sequence similarities

In the C-terminal section; belongs to the GTP cyclohydrolase II family.
In the N-terminal section; belongs to the DHBP synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    420
  • Mass (Da)
    46,489
  • Last updated
    2024-01-24 v1
  • Checksum
    ADB559DA989F8E2F
MTRWERVERAIADFREGKFVIIVDDRDRENEGDLSIAAQHATPQAINFMAREARGLICVPMAPEWADRLGLPLMVPPQANGSRFGTAFTVSVEAREGVTTGISAFDRAVTIQKLAEPASTPADFVTPGHVFPLRARPGGVLERDGQTEASVDLARLAGLHPVAVVCEIMAEDGTMARLPELERFAERHGITLIHVADLIAYRLARERPSLRVAETLLPTEYGDFRIVAYRRFGGEEIDLALIRGEVSGEEPVLVRVHSECLTGDVFGSQRCDCGEQLEAALRLLGEAGRGVLIYLRQEGRGIGLLNKLRAYHLQDQGLDTVEANLELGFPADLRNYREAALILRDLGIQRLRLLTNNPRKVEALSDCGFEIVERVPLEIPANEHNRRYLETKRDKLGHLLQLNGAHPAAELSRAMPGTHD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAMSLR010000002
EMBL· GenBank· DDBJ
MCM8748432.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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